A previous suggestion that BioC may methylate malonyl-ACP instead of malonyl-CoA was confirmed using the BioC enzyme from B. cereus and E. coli malonyl-ACP in vitro because active native BioC cannot be purified; the B. cereus enyzme complements an E. coli bioC mutation thus validating the function of the E. coli BioC enzyme in vivo (Lin, 2012). BioC and BioH are required to synthesize pimeloyl-ACP, a biotin precursor, utilizing the enzymes of fatty acid synthesis to add acyl groups to malonyl-CoA in two cycles to form pimeloyl-ACP methyl ester; BioC may methylate malonyl-ACP instead of malonyl-CoA (Lin, 2010).